1 Introduction To Protein Structure Flashcards

1
Q

Q: What is the simplest amino acid? What is it’s R group?

A

A: Glycine. H

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2
Q

Q: Name 4 amino acids with polar side chains.

A

A: Serine (OH), threonine (OH), Tyrosine (OH), asparagine (CONH2), cysteine (SH)

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3
Q

Q: Are amino acids with polar side chains hydrophilic or hydrophobic?

A

A: Hydrophilic

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4
Q

Q: Which polar amino acid has a 6 carbon ring?

A

A: Tyrosine

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5
Q

Q: Name 3 amino acids with positively charged side chains.

A

A: lysine (NH3+), arginine (NH2NH2 +), histidine (NH in ring)

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6
Q

Q: If an amino acid has a positively charged side chain, is it acidic or basic?

A

A: basic

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7
Q

Q: Name 2 amino acids with negatively charged side chains.

A

A: aspartate and glutamate (COO-)

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8
Q

Q: If an amino acid has a negatively charged side chain, is it acidic or basic?

A

A: Acidic

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9
Q

Q: What travels further during electrophoresis, HbS or HbA?

A

A: HbA as it is more negatively charged (HbA has lost negatively charged glutamate)

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11
Q

Q: What do hydrogen bonds form between?

A

A: CO and NH

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12
Q

Q: What is a peptide bond?

A

A: C=O
I
H- N

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13
Q

Q: What form are amino acids found in proteins?

A

A: L

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14
Q

Q: What is there no free rotation round?

A

A: peptide bond

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15
Q

Q: What causes a kink in an alpha helix peptide chain?

A

A: Proline, NH is lost when it joins and therefore it can’t form a H bond with CO with another part of helix

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16
Q

Q: How does warfarin work?

A

A: prevents carboxylation reaction which is vital in blood clotting cascade of glutamate (post translational mod)

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17
Q

Q: What leads to novel amino acids?

A

A: carboxylation or other post translational mod

18
Q

Q: Compare HbS and HbA.

A

A: Sickle Cell hemoglobin, replacement of a negatively-charged Glu in the standard HbA beta-globin by a neutral Val in HbS results in a protein with a slightly reduced negative charge